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SaRD, a new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties.
Biochem Biophys Res Commun. 1995 Sep 14; 214(2):646-52.BB

Abstract

We have isolated the thermostable 9 kDa SaRD-protein from Sulfolobus acidocaldarius which exhibit RNase activity as well as DNA-binding properties (SaRD). The amino acid composition and the sequence of the 16 N-terminal amino acids show similarities to different RNases as well as to DNA-binding proteins from thermophilic archea. The RNase activity was demonstrated by 5S rRNA degradation, thin layer chromatography and a zymogram. The temperature optimum for the RNase activity is 65 degrees C. The pH optimum ranges from 6.5-7.0. DNA-binding properties were shown by gel-shift assays on agarose gels. In a similar way SaRD mediated protection of DNA against DNase I digestion and Sau3A I restriction could be demonstrated. The melting point (Tm) of genomic DNA was raised from 68 degrees C to 90 degrees C by addition of the SaRD-protein. CD spectroscopy indicated that SaRD is very stable near neutral pH and can neither be unfolded by temperatures up to 85% C nor by addition of 8 M urea.

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Authors+Show Affiliations

Kulms D
Institut für Biochemie, Medizinische Universität zu Lübeck, FRG.
Schäfer G
No affiliation info available
Hahn U
No affiliation info available

MeSH

Amino AcidsChromatography, AffinityChromatography, GelChromatography, Ion ExchangeDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEnzyme StabilityHot TemperatureKineticsMolecular WeightProtein DenaturationProtein FoldingRNA, BacterialRNA, Ribosomal, 5SRibonucleasesSubstrate SpecificitySulfolobus acidocaldarius

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7545905

Citation

Kulms, D, et al. "SaRD, a New Protein Isolated From the Extremophile Archaeon Sulfolobus Acidocaldarius, Is a Thermostable Ribonuclease With DNA-binding Properties." Biochemical and Biophysical Research Communications, vol. 214, no. 2, 1995, pp. 646-52.
Kulms D, Schäfer G, Hahn U. SaRD, a new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties. Biochem Biophys Res Commun. 1995;214(2):646-52.
Kulms, D., Schäfer, G., & Hahn, U. (1995). SaRD, a new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties. Biochemical and Biophysical Research Communications, 214(2), 646-52.
Kulms D, Schäfer G, Hahn U. SaRD, a New Protein Isolated From the Extremophile Archaeon Sulfolobus Acidocaldarius, Is a Thermostable Ribonuclease With DNA-binding Properties. Biochem Biophys Res Commun. 1995 Sep 14;214(2):646-52. PubMed PMID: 7545905.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - SaRD, a new protein isolated from the extremophile archaeon Sulfolobus acidocaldarius, is a thermostable ribonuclease with DNA-binding properties. AU - Kulms,D, AU - Schäfer,G, AU - Hahn,U, PY - 1995/9/14/pubmed PY - 1995/9/14/medline PY - 1995/9/14/entrez SP - 646 EP - 52 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 214 IS - 2 N2 - We have isolated the thermostable 9 kDa SaRD-protein from Sulfolobus acidocaldarius which exhibit RNase activity as well as DNA-binding properties (SaRD). The amino acid composition and the sequence of the 16 N-terminal amino acids show similarities to different RNases as well as to DNA-binding proteins from thermophilic archea. The RNase activity was demonstrated by 5S rRNA degradation, thin layer chromatography and a zymogram. The temperature optimum for the RNase activity is 65 degrees C. The pH optimum ranges from 6.5-7.0. DNA-binding properties were shown by gel-shift assays on agarose gels. In a similar way SaRD mediated protection of DNA against DNase I digestion and Sau3A I restriction could be demonstrated. The melting point (Tm) of genomic DNA was raised from 68 degrees C to 90 degrees C by addition of the SaRD-protein. CD spectroscopy indicated that SaRD is very stable near neutral pH and can neither be unfolded by temperatures up to 85% C nor by addition of 8 M urea. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/7545905/SaRD_a_new_protein_isolated_from_the_extremophile_archaeon_Sulfolobus_acidocaldarius_is_a_thermostable_ribonuclease_with_DNA_binding_properties_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(85)72335-2 DB - PRIME DP - Unbound Medicine ER -